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  Crystal structure of coagulogen, the clotting protein from horseshoe crab - a structural homologue of nerve growth factor

Bergner, A., Oganessyan, V., Muta, T., Iwanaga, S., Typke, D., Huber, R., et al. (1996). Crystal structure of coagulogen, the clotting protein from horseshoe crab - a structural homologue of nerve growth factor. EMBO Journal, 15(24), 6789-6797.

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Bergner, A., Author
Oganessyan, V., Author
Muta, T., Author
Iwanaga, S., Author
Typke, Dieter1, Author              
Huber, R.2, Author              
Bode, Wolfram2, Author              
Affiliations:
1Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565142              
2Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565155              

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Free keywords: Crystal structure; Cystine knot; Horseshoe crab; Nerve growth factor; Spatzle.; Human chorionic-gonadotropin; Proclotting enzyme; Factor superfamily; Rotation function; Drosophila; Similarities; Polarity; Activation; Resolution; Sequence.; Molecular biology & genetics.
 Abstract: The clotting cascade system of the horseshoe crab (Limulus) is involved in both haemostasis and host defence, The cascade results in the conversion of coagulogen, a soluble protein, into an insoluble coagulin gel, The clotting enzyme excises the fragment peptide C from coagulogen, giving rise to aggregation of the monomers, The crystal structure of coagulogen reveals an elongated molecule that embraces the helical peptide C fragment, Cleavage and removal of the peptide C would expose an extended hydrophobic cove, which could interact with the hydrophobic edge of a second molecule, leading to a polymeric fibre. The C-terminal half of the coagulogen molecule exhibits a striking topological similarity to the neurotrophin nerve growth factor (NGF), providing the first evidence for a neurotrophin fold in invertebrates, Similarities between coagulogen and Spatzle, the Drosophila ligand of the receptor Toll, suggest that the neurotrophin fold might be considered more ancient and widespread than previously realized. [References: 55]

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 Dates: 1996-12-16
 Publication Status: Published in print
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 Rev. Type: -
 Identifiers: eDoc: 318692
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Title: EMBO Journal
Source Genre: Journal
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Pages: - Volume / Issue: 15 (24) Sequence Number: - Start / End Page: 6789 - 6797 Identifier: -